ID   GPDA1_ARATH             Reviewed;         400 AA.
AC   Q9SCX9; Q8RXI6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] 1, chloroplastic;
DE            EC=1.1.1.8;
DE   Flags: Precursor;
GN   Name=DHAPRD; OrderedLocusNames=At5g40610; ORFNames=MNF13.16;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RA   Wei Y., Periappuram C., Datla R., Selvaraj G., Zou J.;
RT   "Molecular and biochemical characterizations of a plastidic glycerol-3-
RT   phosphate dehydrogenase from Arabidopsis.";
RL   Plant Physiol. Biochem. 39:841-848(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: Involved in glycerolipid metabolism. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:57945; EC=1.1.1.8;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12.8 uM for glycerone phosphate {ECO:0000269|Ref.1};
CC         Vmax=3.2 umol/sec/mg enzyme toward glycerone phosphate
CC         {ECO:0000269|Ref.1};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed in young seedlings, flowers and siliques.
CC       Expressed at low levels in roots. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AJ242602; CAB64726.1; -; mRNA.
DR   EMBL; AB009052; BAB08532.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94573.1; -; Genomic_DNA.
DR   EMBL; BT000967; AAN41367.1; -; mRNA.
DR   EMBL; AY080863; AAL87336.1; -; mRNA.
DR   RefSeq; NP_198877.1; NM_123425.5.
DR   AlphaFoldDB; Q9SCX9; -.
DR   SMR; Q9SCX9; -.
DR   STRING; 3702.Q9SCX9; -.
DR   PaxDb; 3702-AT5G40610-1; -.
DR   ProteomicsDB; 248463; -.
DR   EnsemblPlants; AT5G40610.1; AT5G40610.1; AT5G40610.
DR   GeneID; 834060; -.
DR   Gramene; AT5G40610.1; AT5G40610.1; AT5G40610.
DR   KEGG; ath:AT5G40610; -.
DR   Araport; AT5G40610; -.
DR   TAIR; AT5G40610; GPDHP.
DR   eggNOG; KOG2711; Eukaryota.
DR   HOGENOM; CLU_033449_2_2_1; -.
DR   InParanoid; Q9SCX9; -.
DR   OMA; YDTPPMD; -.
DR   OrthoDB; 3675564at2759; -.
DR   PhylomeDB; Q9SCX9; -.
DR   UniPathway; UPA00940; -.
DR   PRO; PR:Q9SCX9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9SCX9; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006168; G3P_DH_NAD-dep.
DR   InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR   InterPro; IPR017751; G3P_DH_NAD-dep_euk.
DR   InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR03376; glycerol3P_DH; 1.
DR   PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11728:SF8; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)]-RELATED; 1.
DR   Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR   PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR   PRINTS; PR00077; GPDHDRGNASE.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
DR   Genevisible; Q9SCX9; AT.
PE   1: Evidence at protein level;
KW   Chloroplast; Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..400
FT                   /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] 1,
FT                   chloroplastic"
FT                   /id="PRO_0000287871"
FT   ACT_SITE        257
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         61..66
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         321..322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         352
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   400 AA;  43791 MW;  9A37BC876E8663CC CRC64;
     MRFRSFFFSS SIFSLSHSRS PSLSSSRFSS LSAAMSPALE KSRQGNGGCN DDSKSKVTVV
     GSGNWGSVAA KLIASNALKL PSFHDEVRMW VFEEVLPNGE KLNDVINKTN ENVKYLPGIK
     LGRNVVADPD LENAVKDANM LVFVTPHQFM DGICKKLDGK ITGDVEAISL VKGMEVKKEG
     PCMISSLISK QLGINCCVLM GANIANEIAV EKFSEATVGY RGSREIADTW VQLFSTPYFM
     VTPVHDVEGV ELCGTLKNVV AIAAGFVDGL EMGNNTKAAI MRIGLREMKA LSKLLFPSVK
     DSTFFESCGV ADVITTCLGG RNRRVAEAFA KSRGKRSFDE LEAEMLQGQK LQGVSTAREV
     YEVLKHCGWL EMFPLFSTVH QICTGRLQPE AIVQYRENKL
//